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[ The Protein Srebp2 Drives Cholesterol Formation In Prion-Infected Neuronal Cells Which May Promote Prion-Dependent Diseases ]

The Protein Srebp2 Drives Cholesterol Formation In Prion-Infected Neuronal Cells Which May Promote Prion-Dependent Diseases

Prions are causing fatal and infectious diseases of the nervous system, such as the mad cow disease (BSE), scrapie in sheep or Creutzfeldt-Jakob disease in humans. Scientists of Helmholtz Zentrum Mà nchen and Technische Università t Mà nchen have now succeeded in elucidating another disease mechanism of prion diseases: The prion-infected cell changes its gene expression and produces increased quantities of cholesterol. Prions need this for their propagation. Prions are infectious and transform the brains of humans and animals into sponge-like structures. Unlike a virus, a prion only consists of protein - called prion-protein in its pathological form (PrPSc). Until now, little was known about the processes that take place inside the infected neuronal cell. This made it difficult to develop effective drugs against prion diseases.

Brain Disease Resistance Gene Could Offer Insights Into CJD

A community in Papua New Guinea that suffered a major epidemic of a CJD-like fatal brain disease called kuru has developed strong genetic resistance to the disease, according to new research by Medical Research Council (MRC) scientists. Kuru is a fatal prion disease, similar to CJD in humans and BSE in animals, and is geographically unique to an area in Papua New Guinea. In the mid 20th Century, an epidemic of kuru devastated a population in the Eastern Highlands of Papua New Guinea. The infection was passed on at mortuary feasts, where mainly women and children consumed their deceased relatives as a mark of respect and mourning. This practice was banned and ceased in the late 1950s. Scientists from the MRC Prion Unit, a national centre of excellence in prion diseases, assessed over 3000 people from the affected and surrounding Eastern Highland populations, including 709 who had participated in cannibalistic mortuary feasts, 152 of whom subsequently died of kuru.

Leeds Research Finds New Piece Of BSE Puzzle

New research funded mainly through the Wellcome Trust with additional support from the Medical Research Council shows that a new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease ( CJD ) could be a step closer. The research carried out by scientists at the University of Leeds was published today (November 20) in PLoS Pathogens. The team have found that a protein called Glypican-1 plays a key role in the development of BSE - otherwise known as Mad Cow Disease. BSE is known to be caused by an infectious and abnormal form of the prion protein which is present on cells within the nervous system. But scientists have been unclear as to what causes the prions to become abnormal. The new research from Leeds' Faculty of Biological Sciences provides part of the answer.

Researchers Find New Piece Of BSE Puzzle

A new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease ( CJD ) could be a step closer based on new results from scientists at the University of Leeds. The team has found that a protein called Glypican-1 plays a key role in the development of BSE. Details are published November 20 in the open-access journal PLoS Pathogens. BSE, commonly known as mad cow disease, is known to be caused by an infectious and abnormal form of the prion protein that is present on cells within the nervous system. But scientists have been unclear as to what causes the abnormality to occur. The new research from Leeds' Faculty of Biological Sciences provides part of the answer. The researchers have shown that the presence of Glypican-1 causes the numbers of abnormal prion proteins to rise.

SaBTO Recommends Use Of P-Capt R Prion Reduction Filter To Protect Children From VCJD Blood Transmission

ProMetic Life Sciences Inc. (TSX:PLI) ("ProMetic") and MacoPharma SA ("MacoPharma") announce that the Advisory Committee on the Safety of Blood, Tissues and Organs ("SaBTO"), an independent Committee that advises the UK Department of Health ("DoH"), has recommended the adoption of the P-Capt® prion reduction filter to pre-treat red blood cells destined for children born since 1 January 1996. The filter, which 'cleans' blood prior to use, removes the prion responsible for variant Creutzfeldt-Jakob disease ("vCJD"). The Committee also indicated that the requirement for prion filtration should be reviewed in the event that further data on vCJD prevalence or filter efficacy becomes available. The SaBTO recommendation is subject to the satisfactory completion of the PRISM study, a multi-centre clinical trial initiated in 2007 to evaluate the safety of P-Capt®

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